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Q9HH09 (GLNA_SULAC) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamine synthetase

Short name=GS
EC=6.3.1.2
Alternative name(s):
Glutamate--ammonia ligase
Gene names
Name:glnA
Ordered Locus Names:Saci_1483
OrganismSulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) [Complete proteome] [HAMAP]
Taxonomic identifier330779 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine.

Enzyme regulation

The activity of this enzyme is controlled by adenylation under conditions of abundant glutamine. The fully adenylated enzyme complex is inactive By similarity.

Subunit structure

Dodecamer.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the glutamine synthetase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglutamine biosynthetic process

Inferred from electronic annotation. Source: InterPro

nitrogen fixation

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-ammonia ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 473473Glutamine synthetase
PRO_0000153213

Amino acid modifications

Modified residue4021O-AMP-tyrosine By similarity

Experimental info

Sequence conflict1851D → V in CAC20905. Ref.1
Sequence conflict204 – 2074FTIE → TIEA Ref.1
Sequence conflict2091A → H Ref.1
Sequence conflict211 – 25949HEVAT…FMPKP → EVATAGQGDIDFRFSTLADT ADKVQVLKYVTKNIASKRGM IATFMPKPF Ref.1
Sequence conflict261 – 29939FGDNG…QIGRY → GDNGSGMHTHFSLWTKDGKN LMYDPNDEYAELSQIGRYI Ref.1
Sequence conflict301 – 3033IGG → GPL Ref.1
Sequence conflict305 – 31410LEHGRALSAI → EHGRALSAIV Ref.1
Sequence conflict3171P → G Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9HH09 [UniParc].

Last modified August 30, 2005. Version 2.
Checksum: F8EA4FD71B1CDD5D

FASTA47353,586
        10         20         30         40         50         60 
MPGLPKNEHE ALEFLKSNNI KWVDLQFTDL LGKLQHITIP SNEFDESSFK VGFGKLDGSS 

        70         80         90        100        110        120 
IKGFTSIYES DMVLLPIPQT MTLIPWMQGV ARVLTKVFWG GGKGRFERDP RGIAEEAEKY 

       130        140        150        160        170        180 
QSEQGYVSYF GPELEFFVFD KVEVDASLPQ SGTGYKIHSR EAPWSKNGGY VIRYKEGYYP 

       190        200        210        220        230        240 
ASPVDQLMDI RLEIISTLVD YFGFTIEAAH HEVATAGQGE IDFRFSTLAD TADKVQVLKY 

       250        260        270        280        290        300 
VTKNIASKRG MIATFMPKPF FGDNGSGMHT HFSLWTKDGK NLMYDPNDEY AELSQIGRYI 

       310        320        330        340        350        360 
IGGLLEHGRA LSAIVAPTTN SYRRLVPGYE APVYLVWSKS NRSAAIRIPA YYKGMEKAKR 

       370        380        390        400        410        420 
LEYRPPDPSS NPYLVFSAIL MAGLDGIRRK LDPGDPVDEN IYHMSEEKKR SLKIRELPGS 

       430        440        450        460        470 
LDEALNELES DNEFLKPVFN SSILQAYLDL KKEEAKMMQL YPHPMEIYQY LDS 

« Hide

References

« Hide 'large scale' references
[1]"The glutamine synthetase from the hyperthermoacidophilic crenarcheon Sulfolobus acidocaldarius: isolation, characterization and sequencing of the gene."
Yin Z.M., Purschke W.G., Schaefer G., Schmidt C.L.
Biol. Chem. 379:1349-1354(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
Strain: ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770.
[2]"The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota."
Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E., Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.
J. Bacteriol. 187:4992-4999(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ224678 Genomic DNA. Translation: CAC20905.1.
CP000077 Genomic DNA. Translation: AAY80804.1.
RefSeqYP_256097.1. NC_007181.1.

3D structure databases

ProteinModelPortalQ9HH09.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING330779.Saci_1483.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAY80804; AAY80804; Saci_1483.
GeneID3474677.
KEGGsai:Saci_1483.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0174.
HOGENOMHOG000005157.
KOK01915.
OMAVECQHHE.
ProtClustDBCLSK883635.

Enzyme and pathway databases

BioCycSACI330779:GH9J-1458-MONOMER.
BRENDA6.3.1.2. 6160.

Family and domain databases

Gene3D3.10.20.70. 1 hit.
3.30.590.10. 1 hit.
InterProIPR008147. Gln_synt_beta.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
IPR004809. Gln_synth_I.
IPR027302. Gln_synth_N_conserv_site.
[Graphical view]
PfamPF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view]
SUPFAMSSF54368. SSF54368. 1 hit.
TIGRFAMsTIGR00653. GlnA. 1 hit.
PROSITEPS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLNA_SULAC
AccessionPrimary (citable) accession number: Q9HH09
Secondary accession number(s): Q4J8S1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: August 30, 2005
Last modified: October 16, 2013
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families